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EX7S_ECOLI
ID   EX7S_ECOLI              Reviewed;          80 AA.
AC   P0A8G9; P22938; Q2MC04;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Exodeoxyribonuclease 7 small subunit {ECO:0000255|HAMAP-Rule:MF_00337};
DE            EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00337, ECO:0000269|PubMed:4602029, ECO:0000269|PubMed:4602030};
DE   AltName: Full=Exodeoxyribonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337, ECO:0000303|PubMed:4602029};
DE            Short=ExoVII small subunit;
DE            Short=Exonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337, ECO:0000303|PubMed:4602029};
GN   Name=xseB {ECO:0000255|HAMAP-Rule:MF_00337}; Synonyms=yajE;
GN   OrderedLocusNames=b0422, JW0412;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2089044; DOI=10.1093/oxfordjournals.jbchem.a123327;
RA   Fujisaki S., Hara H., Nishimura Y., Horiuchi K., Nishino T.;
RT   "Cloning and nucleotide sequence of the ispA gene responsible for farnesyl
RT   diphosphate synthase activity in Escherichia coli.";
RL   J. Biochem. 108:995-1000(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-22.
RA   Diaz D.L., Williams K.R., Chase J.W.;
RL   Unpublished observations (AUG-1995).
RN   [6]
RP   IDENTIFICATION OF GENE.
RA   Diaz D.L., Chase J.W.;
RL   Unpublished observations (FEB-1994).
RN   [7]
RP   CATALYTIC ACTIVITY, NO COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12;
RX   PubMed=4602029; DOI=10.1016/s0021-9258(19)42453-8;
RA   Chase J.W., Richardson C.C.;
RT   "Exonuclease VII of Escherichia coli. Purification and properties.";
RL   J. Biol. Chem. 249:4545-4552(1974).
RN   [8]
RP   CATALYTIC ACTIVITY.
RC   STRAIN=K12;
RX   PubMed=4602030; DOI=10.1016/s0021-9258(19)42454-x;
RA   Chase J.W., Richardson C.C.;
RT   "Exonuclease VII of Escherichia coli. Mechanism of action.";
RL   J. Biol. Chem. 249:4553-4561(1974).
RN   [9]
RP   FUNCTION, IDENTIFICATION OF GENE, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=K12;
RX   PubMed=6284744; DOI=10.1016/s0021-9258(18)34201-7;
RA   Vales L.D., Rabin B.A., Chase J.W.;
RT   "Subunit structure of Escherichia coli exonuclease VII.";
RL   J. Biol. Chem. 257:8799-8805(1982).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=22718974; DOI=10.1093/nar/gks547;
RA   Poleszak K., Kaminska K.H., Dunin-Horkawicz S., Lupas A., Skowronek K.J.,
RA   Bujnicki J.M.;
RT   "Delineation of structural domains and identification of functionally
RT   important residues in DNA repair enzyme exonuclease VII.";
RL   Nucleic Acids Res. 40:8163-8174(2012).
RN   [11]
RP   FUNCTION IN MSDNA PROCESSING, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=26626352; DOI=10.1007/s12275-015-5304-0;
RA   Jung H., Liang J., Jung Y., Lim D.;
RT   "Characterization of cell death in Escherichia coli mediated by XseA, a
RT   large subunit of exonuclease VII.";
RL   J. Microbiol. 53:820-828(2015).
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC       insoluble oligonucleotides, which are then degraded further into small
CC       acid-soluble oligonucleotides. It can degrade 3' or 5' ss regions
CC       extending from the termini of duplex DNA molecules and displaced ss
CC       regions. It can also excise thymine dimers in vitro (PubMed:4602029,
CC       PubMed:4602030, PubMed:22718974) (Probable). Required for production of
CC       the mature 5'-end of retron Ec78 or Ec83 msDNA. When in excess of the
CC       large subunit, counteracts the large subunit's toxicity
CC       (PubMed:26626352). {ECO:0000269|PubMed:22718974,
CC       ECO:0000269|PubMed:26626352, ECO:0000269|PubMed:4602029,
CC       ECO:0000269|PubMed:4602030, ECO:0000305|PubMed:6284744}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC         direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00337,
CC         ECO:0000269|PubMed:22718974, ECO:0000269|PubMed:4602029,
CC         ECO:0000269|PubMed:4602030};
CC   -!- COFACTOR:
CC       Note=Does not require a metal cofactor. {ECO:0000269|PubMed:4602029};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.8 to 7.9. {ECO:0000269|PubMed:4602029};
CC   -!- SUBUNIT: Heterooligomer composed of two different subunits with an
CC       approximate ratio of 4:1 for small to large subunit (Probable). Also
CC       estimated to have a 6:1 ration for small to large subunits (Probable).
CC       {ECO:0000305|PubMed:22718974, ECO:0000305|PubMed:6284744}.
CC   -!- INTERACTION:
CC       P0A8G9; P64503: yebV; NbExp=4; IntAct=EBI-1116872, EBI-9126792;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00337,
CC       ECO:0000305|PubMed:6284744}.
CC   -!- DISRUPTION PHENOTYPE: No longer processes msDNA correctly (when retron
CC       Ec78 or Ec83 are expressed in the strain).
CC       {ECO:0000269|PubMed:26626352}.
CC   -!- SIMILARITY: Belongs to the XseB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00337}.
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DR   EMBL; D00694; BAA00598.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40178.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73525.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76202.1; -; Genomic_DNA.
DR   PIR; JQ0664; JQ0664.
DR   RefSeq; NP_414956.1; NC_000913.3.
DR   RefSeq; WP_001124935.1; NZ_STEB01000007.1.
DR   AlphaFoldDB; P0A8G9; -.
DR   SMR; P0A8G9; -.
DR   BioGRID; 4259844; 58.
DR   BioGRID; 849458; 1.
DR   ComplexPortal; CPX-4005; Exodeoxyribonuclease VII complex.
DR   DIP; DIP-48031N; -.
DR   IntAct; P0A8G9; 5.
DR   STRING; 511145.b0422; -.
DR   jPOST; P0A8G9; -.
DR   PaxDb; P0A8G9; -.
DR   PRIDE; P0A8G9; -.
DR   EnsemblBacteria; AAC73525; AAC73525; b0422.
DR   EnsemblBacteria; BAE76202; BAE76202; BAE76202.
DR   GeneID; 67416503; -.
DR   GeneID; 945069; -.
DR   KEGG; ecj:JW0412; -.
DR   KEGG; eco:b0422; -.
DR   PATRIC; fig|1411691.4.peg.1855; -.
DR   EchoBASE; EB1090; -.
DR   eggNOG; COG1722; Bacteria.
DR   HOGENOM; CLU_145918_3_3_6; -.
DR   InParanoid; P0A8G9; -.
DR   OMA; PLNDYKG; -.
DR   PhylomeDB; P0A8G9; -.
DR   BioCyc; EcoCyc:EG11098-MON; -.
DR   BioCyc; MetaCyc:EG11098-MON; -.
DR   BRENDA; 3.1.11.6; 2026.
DR   PRO; PR:P0A8G9; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0009318; C:exodeoxyribonuclease VII complex; IPI:ComplexPortal.
DR   GO; GO:0008855; F:exodeoxyribonuclease VII activity; IMP:EcoliWiki.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:ComplexPortal.
DR   GO; GO:0006298; P:mismatch repair; IDA:ComplexPortal.
DR   Gene3D; 1.10.287.1040; -; 1.
DR   HAMAP; MF_00337; Exonuc_7_S; 1.
DR   InterPro; IPR003761; Exonuc_VII_S.
DR   InterPro; IPR037004; Exonuc_VII_ssu_sf.
DR   PANTHER; PTHR34137; PTHR34137; 1.
DR   Pfam; PF02609; Exonuc_VII_S; 1.
DR   PIRSF; PIRSF006488; Exonuc_VII_S; 1.
DR   SUPFAM; SSF116842; SSF116842; 1.
DR   TIGRFAMs; TIGR01280; xseB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase; Nuclease;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.5"
FT   CHAIN           2..80
FT                   /note="Exodeoxyribonuclease 7 small subunit"
FT                   /id="PRO_0000206945"
SQ   SEQUENCE   80 AA;  8952 MW;  8B10380D442CADF4 CRC64;
     MPKKNEAPAS FEKALSELEQ IVTRLESGDL PLEEALNEFE RGVQLARQGQ AKLQQAEQRV
     QILLSDNEDA SLTPFTPDNE
 
 
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